Research workbench
AlphaFold monomer V2.0 prediction for S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase (A9KFQ4)
Analyse AlphaFold monomer V2.0 prediction for S-ADENOSYLMETHIONINE:TRNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9KFQ4
- Type
- protein
- Length
- 343 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB0E05376C9C95241a0229bD9FE1e93d0AacB321F
- Molecule
- S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase
- UniProt
- A9KFQ4
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 27% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase | protein | 343 | 27% helix, 30% strand | A9KFQ4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.67 | 0.90 | 29 | empty |
| 2 | 125 | 0.41 | 0.75 | 19 | empty |
| 3 | 82 | 0.33 | 0.74 | 13 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A9KFQ4
- Elsewhere: UniProt A9KFQ4 · AlphaFold DB A9KFQ4
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